Synthesis of the glycosaminoglycan-protein linkage tetraosyl peptide moieties of betaglycan, which serve as a hexosamine acceptor for enzymatic glycosyl transfer
抄録
Betaglycan, also known as TGF-β type III receptor, is a membrane-anchored proteoglycan, which has two glycosaminoglycan (GAG) attachment sites (López-Casillas et.al. J. Cell Biol. 1994, 124, 557-568). Chondroitin sulfate (CS) or heparan sulfate (HS) can attach to the first site, Ser535, whereas only CS attaches to the second, Ser546. Although the mechanism behind the assembly of CS and HS is not fully understood, it has been reported that the assembly of HS requires not only a cluster of acidic residues but also hydrophobic residues located near the Ser-Gly attachment sites (Esko, J. D. Zhang, L Curr. Opin. Struct. Biol. 1996, 6, 663-670). To further understand the effects of amino acids close to the Ser residues of the GAG-attachment sites on the glycosyltransferases, two tetraosyl peptides derived from the CS attachment sites of betaglycan, GLcA-Gal-Gal-Xyl-SerGlyAspAsnGly (1) and GLcA-Gal-Gal-Xyl-SerGlyAspAsnGlyPheProGly (2), were synthesized, and used as donor substrates for β1,4-N-acetylgalactosaminyltransferase-I (β4GaINAcT-I) and α1,4-N-acetylglucosaminyltransferase-I (α4GlcNAcT-I). Both the chemically synthesized linkage region tetrasaccharides were far better acceptors for β4GalNAcT-I than for α4GlcNAcT-1 in vitro, although they also showed appreciable acceptor activity for α4GlcNAcT-I.
収録刊行物
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- Carbohydrate Research
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Carbohydrate Research 345 (15), 2115-2123, 2010-10-13
Elsevier
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詳細情報 詳細情報について
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- CRID
- 1050845763937170304
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- NII論文ID
- 120002548780
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- HANDLE
- 2115/44158
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- ISSN
- 00086215
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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- IRDB
- CiNii Articles
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